ArticleMicrobial cell factories2019
Constitutive expression and cell-surface display of a bacterial β-mannanase in Lactobacillus plantarum.
Article in Microbial cell factories, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 38 citations in OpenAlex.
- Harnessing CRISPR-Cas9 for Lactobacillus improvement in silage production: current knowledge and future perspectives.Journal of animal science and biotechnology · 2025Review
- Harnessing magnetic cross-linked cell aggregates (CLCAs) for cost-effective preparation of Konjac mannan-oligosaccharide.Microbial cell factories · 2025Article
- A screening setup to streamlineMaterials today. Bio · 2025Article
- The Recombinant Lactobacillus Strains with the Surface-Displayed Expression of Amuc_1100 Ameliorate Obesity in High-Fat Diet-Fed Adult Mice.Bioengineering (Basel, Switzerland) · 2024Article
- Research and application progress of microbial β-mannanases: a mini-review.World journal of microbiology & biotechnology · 2024Review
- Expanding the genetic programmability of Lactiplantibacillus plantarum.Microbial biotechnology · 2024Review
- A novel, non-GMO surface display in Limosilactobacillus fermentum mediated by cell surface hydrolase without anchor motif.BMC microbiology · 2022Article
- Comparison of the Immunogenic Properties ofFrontiers in microbiology · 2022Article
- Development of a whole-cell biocatalyst for diisobutyl phthalate degradation by functional display of a carboxylesterase on the surface of Escherichia coli.Microbial cell factories · 2020Article
- Cell Wall Anchoring of a Bacterial Chitosanase inInternational journal of molecular sciences · 2020Article
- A SH3_5 Cell Anchoring Domain for Non-recombinant Surface Display on Lactic Acid Bacteria.Frontiers in bioengineering and biotechnology · 2020Article
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
Abstract
backgroundLactic acid bacteria (LAB) are important microorganisms in the food and beverage industry. Due to their food-grade status and probiotic characteristics, several LAB are considered as safe and effective cell-factories for food-application purposes. In this present study, we aimed at constitutive expression of a mannanase from Bacillus licheniformis DSM13, which was subsequently displayed on the cell surface of Lactobacillus plantarum WCFS1, for use as whole-cell biocatalyst in oligosaccharide production.
resultsTwo strong constitutive promoters, Pgm and SlpA, from L. acidophilus NCFM and L. acidophilus ATCC4356, respectively, were used to replace the inducible promoter in the lactobacillal pSIP expression system for the construction of constitutive pSIP vectors. The mannanase-encoding gene (manB) was fused to the N-terminal lipoprotein anchor (Lp_1261) from L. plantarum and the resulting fusion protein was cloned into constitutive pSIP vectors and expressed in L. plantarum WCFS1. The localization of the protein on the bacterial cell surface was confirmed by flow cytometry and immunofluorescence microscopy. The mannanase activity and the reusability of the constructed L. plantarum displaying cells were evaluated. The highest mannanase activities on the surface of L. plantarum cells obtained under the control of the Pgm and SlpA promoters were 1200 and 3500 U/g dry cell weight, respectively, which were 2.6- and 7.8-fold higher compared to the activity obtained from inducible pSIP anchoring vectors. Surface-displayed mannanase was shown to be able to degrade galactomannan into manno-oligosaccharides (MOS).
conclusionThis work demonstrated successful displaying of ManB on the cell surface of L. plantarum WCFS1 using constitutive promoter-based anchoring vectors for use in the production of manno-oligosaccharides, which are potentially prebiotic compounds with health-promoting effects. Our approach, where the enzyme of interest is displayed on the cell surface of a food-grade organism with the use of strong constitutive promoters, which continuously drive synthesis of the recombinant protein without the need to add an inducer or change the growth conditions of the host strain, should result in the availability of safe, stable food-grade biocatalysts.
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